Abstract
The 'art' genes encode specific arginine uptake proteins, and are repressed by the repressible promoters of ArgR, affecting transcription of artJ [1,2]. Cpb0502, the arginine-binding periplasmic protein 2 precursor from Chlamydophila pneumoniae TW-183 strains, is responsible for arginine transport. As C. pneumoniae is difficult to isolate and culture, there have been many studies of better ways to detect it. A microimmunofluorescence assay (MIF) is still considered to be the 'gold standard' for detecting C. pneumoniae. Although MIF has its own limitations, a number of immunogenic antigens have been shown to be C. pneumoniae specific by this test. Here, we report Cpb0502 as a specific immunogenic antigen against C. pneumoniae as it was detected only in human infection sera of C. pneumoniae but not in Legionella pneumophila and Mycoplasma pneumoniae infection sera, showing high specificity and sensitivity by MIF, western blot and ELISA analysis. And also the crystal structure of Cpb0502 was determined to be a dimer at 2.07. å, revealing a similar backbone structure to a histidine kinase receptor, HK29S. Therefore we may suggest that Cpb0502 is a candidate immunogenic antigen for better diagnosis of C. pneumoniae.
| Original language | English |
|---|---|
| Pages (from-to) | 518-524 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 418 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2012 Feb 17 |
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Keywords
- Arginine periplasmic binding protein 2
- Chlamydophila pneumoniae
- Diagnosis
- Immunogenic antigen
- Serological test
- Structural analysis
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Molecular Biology
Cite this
Structural analysis and serological test of arginine periplasmic binding protein 2 from Chlamydophila pneumoniae. / Park, Sung Ha; Chang, Ji Eun; Hawkes, Hye Jin Kim; Kang, Yeon Ho; Hwang, Kwang Yeon.
In: Biochemical and Biophysical Research Communications, Vol. 418, No. 3, 17.02.2012, p. 518-524.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural analysis and serological test of arginine periplasmic binding protein 2 from Chlamydophila pneumoniae
AU - Park, Sung Ha
AU - Chang, Ji Eun
AU - Hawkes, Hye Jin Kim
AU - Kang, Yeon Ho
AU - Hwang, Kwang Yeon
PY - 2012/2/17
Y1 - 2012/2/17
N2 - The 'art' genes encode specific arginine uptake proteins, and are repressed by the repressible promoters of ArgR, affecting transcription of artJ [1,2]. Cpb0502, the arginine-binding periplasmic protein 2 precursor from Chlamydophila pneumoniae TW-183 strains, is responsible for arginine transport. As C. pneumoniae is difficult to isolate and culture, there have been many studies of better ways to detect it. A microimmunofluorescence assay (MIF) is still considered to be the 'gold standard' for detecting C. pneumoniae. Although MIF has its own limitations, a number of immunogenic antigens have been shown to be C. pneumoniae specific by this test. Here, we report Cpb0502 as a specific immunogenic antigen against C. pneumoniae as it was detected only in human infection sera of C. pneumoniae but not in Legionella pneumophila and Mycoplasma pneumoniae infection sera, showing high specificity and sensitivity by MIF, western blot and ELISA analysis. And also the crystal structure of Cpb0502 was determined to be a dimer at 2.07. å, revealing a similar backbone structure to a histidine kinase receptor, HK29S. Therefore we may suggest that Cpb0502 is a candidate immunogenic antigen for better diagnosis of C. pneumoniae.
AB - The 'art' genes encode specific arginine uptake proteins, and are repressed by the repressible promoters of ArgR, affecting transcription of artJ [1,2]. Cpb0502, the arginine-binding periplasmic protein 2 precursor from Chlamydophila pneumoniae TW-183 strains, is responsible for arginine transport. As C. pneumoniae is difficult to isolate and culture, there have been many studies of better ways to detect it. A microimmunofluorescence assay (MIF) is still considered to be the 'gold standard' for detecting C. pneumoniae. Although MIF has its own limitations, a number of immunogenic antigens have been shown to be C. pneumoniae specific by this test. Here, we report Cpb0502 as a specific immunogenic antigen against C. pneumoniae as it was detected only in human infection sera of C. pneumoniae but not in Legionella pneumophila and Mycoplasma pneumoniae infection sera, showing high specificity and sensitivity by MIF, western blot and ELISA analysis. And also the crystal structure of Cpb0502 was determined to be a dimer at 2.07. å, revealing a similar backbone structure to a histidine kinase receptor, HK29S. Therefore we may suggest that Cpb0502 is a candidate immunogenic antigen for better diagnosis of C. pneumoniae.
KW - Arginine periplasmic binding protein 2
KW - Chlamydophila pneumoniae
KW - Diagnosis
KW - Immunogenic antigen
KW - Serological test
KW - Structural analysis
UR - http://www.scopus.com/inward/record.url?scp=84863150814&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84863150814&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2012.01.058
DO - 10.1016/j.bbrc.2012.01.058
M3 - Article
C2 - 22285188
AN - SCOPUS:84863150814
VL - 418
SP - 518
EP - 524
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 3
ER -